jats:titleAbstract</jats:title>jats:pThe integration of enzymes with synthetic materials allows efficient electrocatalysis and production of solar fuels. Here, we couple formate dehydrogenase (jats:boldFDH</jats:bold>) from Desulfovibrio vulgaris Hildenborough (DvH) to metal oxides for catalytic COjats:sub2</jats:sub> reduction and report an in‐depth study of the resulting enzyme–material interface. Protein film voltammetry (PFV) demonstrates the stable binding of jats:boldFDH</jats:bold> on metal‐oxide electrodes and reveals the reversible and selective reduction of COjats:sub2</jats:sub> to formate. Quartz crystal microbalance (QCM) and attenuated total reflection infrared (ATR‐IR) spectroscopy confirm a high binding affinity for jats:boldFDH</jats:bold> to the TiOjats:sub2</jats:sub> surface. Adsorption of jats:boldFDH</jats:bold> on dye‐sensitized TiOjats:sub2</jats:sub> allows for visible‐light‐driven COjats:sub2</jats:sub> reduction to formate in the absence of a soluble redox mediator with a turnover frequency (TOF) of 11±1 sjats:sup−1</jats:sup>. The strong coupling of the enzyme to the semiconductor gives rise to a new benchmark in the selective photoreduction of aqueous COjats:sub2</jats:sub> to formate.</jats:p>